3WUH

Qri7 and AMP complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000049	molecular_function	tRNA binding
A	0002949	biological_process	tRNA threonylcarbamoyladenosine modification
A	0005739	cellular_component	mitochondrion
A	0005759	cellular_component	mitochondrial matrix
A	0006400	biological_process	tRNA modification
A	0008033	biological_process	tRNA processing
A	0008252	molecular_function	nucleotidase activity
A	0008270	molecular_function	zinc ion binding
A	0016740	molecular_function	transferase activity
A	0016746	molecular_function	acyltransferase activity
A	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
A	0046872	molecular_function	metal ion binding
A	0061711	molecular_function	tRNA N(6)-L-threonylcarbamoyladenine synthase activity
A	0070525	biological_process	tRNA threonylcarbamoyladenosine metabolic process
A	0072670	biological_process	mitochondrial tRNA threonylcarbamoyladenosine modification
B	0000049	molecular_function	tRNA binding
B	0002949	biological_process	tRNA threonylcarbamoyladenosine modification
B	0005739	cellular_component	mitochondrion
B	0005759	cellular_component	mitochondrial matrix
B	0006400	biological_process	tRNA modification
B	0008033	biological_process	tRNA processing
B	0008252	molecular_function	nucleotidase activity
B	0008270	molecular_function	zinc ion binding
B	0016740	molecular_function	transferase activity
B	0016746	molecular_function	acyltransferase activity
B	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
B	0046872	molecular_function	metal ion binding
B	0061711	molecular_function	tRNA N(6)-L-threonylcarbamoyladenine synthase activity
B	0070525	biological_process	tRNA threonylcarbamoyladenosine metabolic process
B	0072670	biological_process	mitochondrial tRNA threonylcarbamoyladenosine modification

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 501

Chain	Residue
A	HIS145
A	HIS149
A	HIS175
A	ASP361

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site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE AMP A 502

Chain	Residue
A	GLU221
A	GLY325
A	VAL326
A	SER328
A	ASN329
A	MET356
A	CYS359
A	SER360
A	HOH601
A	SER172
A	GLY173
A	GLY199
A	ASP203
A	ALA217

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site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE ZN B 501

Chain	Residue
B	HIS145
B	HIS149
B	HIS175
B	ASP361
B	HOH601

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site_id	AC4
Number of Residues	14
Details	BINDING SITE FOR RESIDUE AMP B 502

Chain	Residue
B	SER172
B	GLY173
B	GLY199
B	ASP203
B	MET215
B	ALA217
B	ARG218
B	GLU221
B	GLY325
B	VAL326
B	SER328
B	ASN329
B	SER360
B	ASP361

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Functional Information from PROSITE/UniProt

site_id	PS01016
Number of Residues	21
Details	GLYCOPROTEASE Glycoprotease family signature. KGlavaWNkPlIgvhHmlGHL

Chain	Residue	Details
A	LYS130-LEU150

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03179","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23620299","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03179","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25084372","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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